ID F1RUH0_PIG Unreviewed; 4415 AA.
AC F1RUH0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=HUWE1 {ECO:0000313|Ensembl:ENSSSCP00000013120.3,
GN ECO:0000313|VGNC:VGNC:89008};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000013120.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000013120.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000013120.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDA53594.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000013120.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR EMBL; DQIR01098118; HDA53594.1; -; Transcribed_RNA.
DR RefSeq; XP_005673709.1; XM_005673652.2.
DR STRING; 9823.ENSSSCP00000013120; -.
DR Ensembl; ENSSSCT00000013481.5; ENSSSCP00000013120.3; ENSSSCG00000012328.6.
DR GeneID; 100517442; -.
DR KEGG; ssc:100517442; -.
DR CTD; 10075; -.
DR VGNC; VGNC:89008; HUWE1.
DR eggNOG; KOG0939; Eukaryota.
DR GeneTree; ENSGT00940000156319; -.
DR OrthoDB; 5396290at2759; -.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008227; Chromosome X.
DR Bgee; ENSSSCG00000012328; Expressed in medulla oblongata and 41 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0140852; F:histone ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IEA:Ensembl.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd14288; UBA_HUWE1; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041918; UBA_HUWE1.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50918; WWE; 1.
PE 1: Evidence at protein level;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1RUH0};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1357..1396
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1644..1721
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 4079..4415
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 748..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2303..2382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2397..2520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2735..3011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3077..3100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3282..3308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3395..3423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3446..3466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3512..3552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3577..3607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3778..3799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3822..3889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3952..3972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2059..2076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2077..2101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2303..2336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2425..2443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2447..2512
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2735..2759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2760..2810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2856..2930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2959..2975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3082..3100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3285..3301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3512..3549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3824..3840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3854..3871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4382
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4415 AA; 486172 MW; 22B421821B24B48C CRC64;
MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE LYHWVDLLDR
FDGILADAGQ TVENMSWMLV CDRPEREQLK MLLLAVLNFT ALLIEYSFSR HLYSSIEHLT
TLLASSDMQV VLAVLNLLYV FSKRSNYITR LGSDKRTPLL TRLQHLAESW GGKENGFGLA
ECCRDLHMMK YPPSATTLHF EFYADPGAEV KIEKRTTSNT LHYIHIEQLD KISESPSEIM
ESLTKMYSIP KDKQMLLFTH IRLAHGFSNH RKRLQAVQAR LHAISILVYS NALQESANSI
LYNGLIEELV DVLQITDKQL MEIKAASLRT LTSIVHLERT PKLSSIIDCT GTASYHGFLP
VLVRNCIQAM IDPSMDPYPH QFATALFSFL YHLASYDAGG EALVSCGMME ALLKVIKFLG
DEQDQITFVT RAVRVVDLIT NLDMAAFQSH SGLSIFIYRL EHEVDLCRKE CPFVIKPKIQ
RPSTTQEGEE METDVDVADV TMESSPGSSI SMEHRLDVEL RASSSSSTSI SSGPGPRPGV
QCIPQRAALL KSMLNFLKKA IQDPAFSDGI RHVMDGSLPT SLKHIISNAE YYGPSLFLLA
TEVVTVFVFQ EPSLLSSLQD NGLTDVMLHA LLIKDVPATR EVLGSLPNVF SALCLNARGL
QSFVQCQPFE RLFKVLLSPD YLPAMRRRRS SDPLGDTASN LGSAVDELMR HQPTLKTDAT
TAIIKLLEEI CNLGRDPKYI CQKPSIQKAD GTATAPPPRS NHAAEEASSE DEEEEEVQAM
QSFNSTQQNE TEPNQQVVGT EERIPIPLMD YILNVMKFVE SILSNNTTDD HCQEFVNQKG
LLPLVTILGL PNLPIDFPTS AACQAVAGVC KSILTLSHEP KVLQEGLLQL DSILSSLEPL
HRPIESPGGS VLLRELACAG NVADATLSAQ ATPLLHALTA AHAYIMMFVH TCRVGQSEIR
SISVNQWGSQ LGLSVLSKLS QLYCSLVWES TVLLSLCTPN SLPSGCEFGQ ADMQKLVPKD
EKAGTTQGGK RSDGEQDGTA GSMDASTQGL LEGIGLDGDT LAPMETDEPA SDSKGKSKIT
PAMAARIKQI KPLLSASSRL GRALAELFGL LVKLCVGSPV RQRRSHHAAS TTTAPTPAAR
STASALTKLL TKGLSWQPPP YTPTPRFRLT FFICSVGFTS PMLFDERKYP YHLMLQKFLC
SGGHNALFET FNWALSMGGK VPVAEGLEHS DLPDGTGEFL DAWLMLVEKM VNPTTVLESP
HSLPAKLPGG VQNFPQFSAL RFLVVTQKAA FTCIKNLWNR KPLKVYGGRM AESMLAILCH
ILRGEPVIRE RLSKEKEGSR GEEDTGQEEG GSRREPQVNQ QQLQQLMDMG FTREHAMEAL
LNTSTMEQAT EYLLTHPPPI MGGVVRDLSM SEEDQMMRAI AMSLGQDIPM DQRAESPEEV
ACRKEEEERK AREKQEEEEA KCLEKFQDAD PLEQDELHTF TDTMLPGCFH LLDELPDTVY
RVCDLIMTAI KRNGADYRDM ILKQVVNQVW EAADVLIKAA LPLTTSDTKT VSEWISQMAT
LPQASNLATR ILLLTLLFEE LKLPCAWVVE SSGILNVLIK LLEVVQPCLQ AAKEQKEVQT
PKWITPVLLL IDFYEKTAIS SKRRAQMTKY LQSNNNNWRW FDDRSGRWCS YSASNNSTID
SAWKSGETSV RFTAGRRRYT VQFTTMVQVN EETGNRRPVM LTLLRVPRLN KNSKNSNGQE
LEKTLEESKE MDIKRKENKA NDTPLALDST NTEKETSLEE TKIGEILIQG LTEDMVTVLI
RACVSMLGVP VDPDTLHATL RLCLRLTRDH KYAMMFAELK STRMILNLTQ SSGFNGFTPL
VTLLLRHIIE DPCTLRHTME KVVRSAATSG AGSTTSGVVS GSLGSREINY ILRVLGPAAC
RNPDIFTEVA NCCIRIALPA PRGSGTASDD EFENLRIKGP NAVQLVKTTP LKPSPLPVIP
DTIKEVIYDM LNALAAYHAP EEADKSDPKP GGMTQEVGQL LQDMGDDVYQ QYRSLTRQSS
DFDTQSGFSI NSQVFAADGA STETSTSGTS QGEASTPEES RDGKKDKEGD RASEEGKQKG
KGSKPLMPTS TILRLLAELV RSYVGIATLI ANYSYTVGQS ELIKEDCSVL AFVLDHLLPH
TQNAEDKDTP ALARLFLASL AAAGSGTDAQ VALVNEVKAA LGRALAMAES TEKHARLQAV
MCIISTIMES CPSTSSFYSS ATAKTQHNGM NNIIRLFLKK GLVNDLARVP HSLDLSSPNM
ANTVNAALKP LETLSRIVNQ PSSLFGSKSA SSKSKSEQDA QGAAQDSNSN QQDPGEPGEA
EVQEEDHDVT QTEVADGDIM DGEAETDSVV IAGQPEVLSS QEMQVENELE DLIDELLERD
GGSGNSTIIV SRSGEDESQE DVLMDEAPSN LSQASTLQAN REDSMNILDP EDEEEHTQEE
DSSGSNEDED DSQDEEEEEE EDEEDDQEDD EGEEGDEDDD DDGSEMELDE DYPDMNASPL
VRFERFDRED DLIIEFDNMF SSATDIPPSP GNIPTTHPLM VRHADHSSLT LGSGSSTTRL
TQGIGRSQRT LRQLTANTGH TIHVHYPGNR QPNPPLILQR LLGPSAAADI LQLSSSLPLQ
SRGRARLLVG NDDVHIIARS DDELLDDFFH DQSTATSQAG TLSSIPTALT RWTEECKVLD
AESMHDCVSV VKVPIVNHLE FLRDEELEER REKRRKQLAE EETKITDKGK EDKENRDQSA
QCTASKTNDS TEQNLSDGTP MPDSYPTTPS STDAATSEPK ETLVTLQPSQ QQPTLPPPPA
LGEIPQELQS PTGEGGSSTQ LLMPVEPEEL GPTRPSGEAE TTQMELSPAP TITSLSPERA
EDSDALTAVS SQLEGSPMDT SSLASCTLEE AVGDTSAAGS SEQPTAGSST PGDAPPVVPD
VQGRGDGSGE PTQPPEDSSP PASSESSSTR DSAVAISGAD SRGILEEPLP STSSEEEDPL
AGISLPEGVD PSFLAALPDD IRREVLQNQL GIRPPTRTAP STNSSAPAVV GNPGVTEVSP
EFLAALPPAI QEEVLAQQRA EQQRRELAQN ASSDTPMDPV TFIQTLPSDL RRSVLEDMED
SVLAVMPPDI AAEAQALRRE QEARQRQLMH ERLFGHSSTS ALSAILRSPA FTSRLSGNRG
VQYTRLAVQR GGTFQMGGSS SHNRPSGSNV DTLLRLRGRL LLDHEALSCL LVLLFVDEPK
LNTSRLHRVL RNLCYHAQTR HWVIRSLLSI LQRSSESELC IETPKLSSSE EKGKKSSKSC
GSSSHENRPL DLLHKMESKS SNQLSWLSVS MDAALGCRTN IFQIQRSGGR KHTEKHASSG
STVHIHPQAA PVVCRHVLDT LIQLAKVFPS HFTQQRTKET NCESDRERGS KQACSPCSSQ
STSSGICTDF WDLLVKLDNM NVSRKGKNSV KSVPVSAGGE GETSPYSLEA SPLGQLMNML
SHPVIRRSSL LTEKLLRLLS LISIALPENK VSEAQANSGS SASSTTVATS TTSTTTTTAA
SSTPTPPAAT TPVTSAPALV AATAISTIAV AASTTVTTPT TATTTVSTST TKASKSPAKV
GDMGSSSTDF KMVSSGLTEN QLQLSVEVLT SHSCSEEGLE DAANVLLQLS RGDPGTRDTV
LKLLLNGARH LGYTLCKQIG TLLAELREYN LEQQRRAQCE TLSPDGLPEE QPQTTKLKGK
MQSRFDMAEN VVIVASQKRP LGGRELQLPS MSMLTSKTST QKFFLRVLQV IIQLRDDTRR
ANKKAKQTGR LGSSGLGSAS SIQAAVRQLE AEADAIIQMV REGQRARRQQ QAATSESSQS
EASVRREESP MDVDQPSPSA QDTQSIGSDG TPQGEKEKEE RPPELPLLSE QLSLDELWDM
LGECLKELEE SHDQHAVLVL QPAVEAFFLV HATERESKPP IRDTRESQLA HIKDEPPPLS
PAPLTPATPS SLDPFFSREP SSMHISSSLP PDTQKFLRFA ETHRTVLNQI LRQSTTHLAD
GPFAVLVDYI RVLDFDVKRK YFRQELERLD EGLRKEDMAV HVRRDHVFED SYRELHRKSP
EEMKNRLYIV FEGEEGQDAG GLLREWYMII SREMFNPMYA LFRTSPGDRV TYTINPSSHC
NPNHLSYFKF VGRIVAKAVY DNRLLECYFT RSFYKHILGK SVRYTDMESE DYHFYQGLVY
LLENDVSTLG YDLTFSTEVQ EFGVCEVRDL KPNGANILVT EENKKEYVHL VCQMRMTGAI
RKQLAAFLEG FYEIIPKRLI SIFTEQELEL LISGLPTIDI DDLKSNTEYH KYQSNSIQIQ
WFWRALRSFD QADRAKFLQF VTGTSKVPLQ GFAALEGMNG IQKFQIHRDD RSTDRLPSAH
TCFNQLDLPA YESFEKLRHM LLLAIQECSE GFGLA
//
